Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 28 March 1986:
Vol. 231. no. 4745, pp. 1580 - 1584
DOI: 10.1126/science.2420008

Articles

Science, Vol 231, Issue 4745, 1580-1584
Copyright © 1986 by American Association for the Advancement of Science


articles

HTLV-III gag protein is processed in yeast cells by the virus pol-protease

RA Kramer, MD Schaber, AM Skalka, K Ganguly, F Wong-Staal, and EP Reddy

The gag-pol gene of HTLV-III (human T-lymphotropic virus), the virus linked to AIDS (acquired immune deficiency syndrome), was expressed in yeast, and processing of the gag precursor into proteins of the same size as those in the virion was observed. Processing of the gag gene in yeast cells mimics the process that naturally occurs in mammalian cells during maturation of virions. Therefore it was possible to perform mutational analysis of the virus genome to localize the gene that codes for the protease function to the amino terminal coding region of the pol gene. Since this region overlaps the gag gene, it is likely that ribosomal frameshifting occurs from gag to pol. Antibodies in all of the AIDS patients' sera tested recognized the yeast synthesized gag proteins, although the sera showed differences in relative reactivity to the individual gag proteins and the precursor. This yeast system should be valuable not only for production of viral proteins for diagnostic or vaccine purposes but also for analysis of the genetics and biochemistry of viral gene functions--parameters that are difficult to study otherwise with this virus.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mapping Protease Inhibitor Resistance to Human Immunodeficiency Virus Type 1 Sequence Polymorphisms within Patients.
A. F. Y. Poon, S. L. Kosakovsky Pond, D. D. Richman, and S. D. W. Frost (2007)
J. Virol. 81, 13598-13607
   Abstract »    Full Text »    PDF »
Atazanavir Signature I50L Resistance Substitution Accounts for Unique Phenotype of Increased Susceptibility to Other Protease Inhibitors in a Variety of Human Immunodeficiency Virus Type 1 Genetic Backbones.
S. Weinheimer, L. Discotto, J. Friborg, H. Yang, and R. Colonno (2005)
Antimicrob. Agents Chemother. 49, 3816-3824
   Abstract »    Full Text »    PDF »
Folding Regulates Autoprocessing of HIV-1 Protease Precursor.
A. Chatterjee, P. Mridula, R. K. Mishra, R. Mittal, and R. V. Hosur (2005)
J. Biol. Chem. 280, 11369-11378
   Abstract »    Full Text »    PDF »
Phosphorylation and Proteolytic Cleavage of Gag Proteins in Budded Simian Immunodeficiency Virus.
S. M. Rue, J. W. Roos, P. M. Tarwater, J. E. Clements, and S. A. Barber (2005)
J. Virol. 79, 2484-2492
   Abstract »    Full Text »    PDF »
Hydrogen Bonding at a Conserved Threonine in Lentivirus Capsid Is Required for Virus Replication.
S. M. Rue, J. W. Roos, L. M. Amzel, J. E. Clements, and S. A. Barber (2003)
J. Virol. 77, 8009-8018
   Abstract »    Full Text »    PDF »
HIV type 1 Gag virus-like particle budding from spheroplasts of Saccharomycescerevisiae.
S. Sakuragi, T. Goto, K. Sano, and Y. Morikawa (2002)
PNAS 99, 7956-7961
   Abstract »    Full Text »    PDF »
BMS-232632, a Highly Potent Human Immunodeficiency Virus Protease Inhibitor That Can Be Used in Combination with Other Available Antiretroviral Agents.
B. S. Robinson, K. A. Riccardi, Y.-f. Gong, Q. Guo, D. A. Stock, W. S. Blair, B. J. Terry, C. A. Deminie, F. Djang, R. J. Colonno, et al. (2000)
Antimicrob. Agents Chemother. 44, 2093-2099
   Abstract »    Full Text »
Comparison of Human Immunodeficiency Virus Type 1 Pr55Gag and Pr160Gag-Pol Processing Intermediates That Accumulate in Primary and Transformed Cells Treated with Peptidic and Nonpeptidic Protease Inhibitors.
R. R. Speck, C. Flexner, C.-J. Tian, and X.-F. Yu (2000)
Antimicrob. Agents Chemother. 44, 1397-1403
   Abstract »    Full Text »
Resistance to Human Immunodeficiency Virus Type 1 Protease Inhibitors.
D. Boden and M. Markowitz (1998)
Antimicrob. Agents Chemother. 42, 2775-2783
   Full Text »
HIV-Protease Inhibitors.
C. Flexner (1998)
N. Engl. J. Med. 338, 1281-1293
   Full Text »    PDF »
Analysis of the S3 and S3' subsite specificities of feline immunodeficiency virus (FIV) protease: Development of a broad-based protease inhibitor efficacious against FIV, SIV, and HIV in vitro and ex vivo.
T. Lee, G. S. Laco, B. E. Torbett, H. S. Fox, D. L. Lerner, J. H. Elder, and C.-H. Wong (1998)
PNAS 95, 939-944
   Abstract »    Full Text »    PDF »
Treatment of Human Immunodeficiency Virus Infection with Saquinavir, Zidovudine, and Zalcitabine.
A. C. Collier, R. W. Coombs, D. A. Schoenfeld, R. L. Bassett, J. Timpone, A. Baruch, M. Jones, K. Facey, C. Whitacre, V. J. McAuliffe, et al. (1996)
N. Engl. J. Med. 334, 1011-1018
   Abstract »    Full Text »    PDF »
Molecular targets for AIDS therapy.
H Mitsuya, R Yarchoan, and S Broder (1990)
Science 249, 1533-1544
   Abstract »    PDF »
Rational design of peptide-based HIV proteinase inhibitors.
N. Roberts, J. Martin, D Kinchington, A. Broadhurst, J. Craig, I. Duncan, S. Galpin, B. Handa, J Kay, A Krohn, et al. (1990)
Science 248, 358-361
   Abstract »    PDF »
Molecular modeling of the HIV-1 protease and its substrate binding site.
I. Weber, M Miller, M Jaskolski, J Leis, A. Skalka, and A Wlodawer (1989)
Science 243, 928-931
   Abstract »    PDF »
Unexpectedly high levels of HIV-1 RNA and protein synthesis in a cytocidal infection.
M Somasundaran and H. Robinson (1988)
Science 242, 1554-1557
   Abstract »    PDF »
Reading frame selection and transfer RNA anticodon loop stacking.
J. Curran and M Yarus (1987)
Science 238, 1545-1550
   Abstract »    PDF »
Expression and processing of the AIDS virus reverse transcriptase in Escherichia coli.
W. Farmerie, D. Loeb, N. Casavant, C. Hutchison 3rd, M. Edgell, and R Swanstrom (1987)
Science 236, 305-308
   Abstract »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)